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Q5NZY0 (HUTI_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Imidazolonepropionase
EC=3.5.2.7
Alternative name(s):
Imidazolone-5-propionate hydrolase
Gene names
Name:hutI
Ordered Locus Names:AZOSEA32590
ORF Names:ebA5740
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+. HAMAP MF_00372

Cofactor

Binds 1 zinc or iron ion per subunit By similarity. HAMAP MF_00372

Pathway

Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. HAMAP MF_00372

Subcellular location

Cytoplasm Potential HAMAP MF_00372.

Sequence similarities

Belongs to the HutI family.

Ontologies

Keywords
   Biological processHistidine metabolism
   Cellular componentCytoplasm
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhistidine catabolic process to glutamate and formamide

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionimidazolonepropionase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Imidazolonepropionase HAMAP MF_00372
PRO_0000306427

Sites

Metal binding711Zinc or iron By similarity
Metal binding731Zinc or iron By similarity
Metal binding2411Zinc or iron By similarity
Metal binding3161Zinc or iron By similarity
Binding site801Substrate By similarity
Binding site931Substrate By similarity
Binding site1431Substrate By similarity
Binding site1761Substrate By similarity
Binding site2441Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NZY0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: AE90E6894E27F740

FASTA41243,320
        10         20         30         40         50         60 
MAAWDLLFRR VHLATFAGDE PYGALRDGAL AVRTGRIEWL GAERDLPREA RAAQEIDGAG 

        70         80         90        100        110        120 
GWLLPGLIDC HTHLVHAGNR AREFELRMQG ANYEEIARAG GGIRVTVIAT RAADEAALVV 

       130        140        150        160        170        180 
ASRPRLARLI AEGVTTVEIK SGYGLELSAE RRMLRAARAL GDTAPVRVTT TFLGAHALPP 

       190        200        210        220        230        240 
EYDGRADDYI AEVCDVMLPA LYREGLVDAV DAFCERIAFS PAQTEAVFRA ARALGLPVRL 

       250        260        270        280        290        300 
HAEQLSDSGG AALAARYGAL CADHLEHLSE AGAAALAAAG SVAVLLPGAF YFLRETHLPP 

       310        320        330        340        350        360 
AARLRALGVP VAIATDCNPG TSPLSSLLLA LNMACVLFRL SPAAALAGVT RNAARALGRG 

       370        380        390        400        410 
DDLGTLEAGK LADLGLWNVD TPAELCYHLG YNPLALRVFG GQISGAGDVA QG

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI09384.1.
RefSeqYP_160285.1. NC_006513.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ5NZY0.
SMRQ5NZY0. Positions 5-403.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5NZY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3180956.
GenomeReviewsGene locus AZOSEA32590 in contig CR555306_GR.
KEGGeba:ebA5740.
NMPDRfig|76114.4.peg.3264.
PATRIC20972737. VBIAroAro98752_3289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycASP76114:EBA5740-MONOMER.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_AROAE
AccessionPrimary (citable) accession number: Q5NZY0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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